The mitochondrial permeability transition pore may comprise VDAC molecules: I. Binary structure and voltage dependence of the pore
作者： Ildikó Szabó , Mario Zoratti
DOI: 10.1016/0014-5793(93)80273-W
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摘要: Abstract Electrophysiological records suggest that the pore responsible for mitochondrial Ca2+-dependent permeability transition (FTP), identified as megachannel (MMC) observed in patch-clamp experiments, may comprise two cooperating porin (VDAC) molecules. We have re-investigated voltage dependence of megachannel, which favors closed state(s) at negative (physiological) transmembrane potentials. This behavior confirms MMC corresponds to permeabilization pore. As detailed accompanying paper [(1993) FEBS Lett. 330, 206-210] this resembles VDAC. Alpidem, a ligand benzodiazepine receptor, reportedly comprises VDAC, adenine nucleotide carrier and third component, elicited currents from silent mitoplast patches, suggesting receptor be identical PTP/MMC.
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